Riboflavin kinaza

Riboflavin kinaza (EC 2.7.1.26, flavokinaza, FK, RFK) je enzim sa sistematskim imenom ATP:riboflavin 5'-fosfotransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju

Riboflavin kinaza
PDB 1s4m EBI.jpg
Identifikatori
EC broj 2.7.1.26
CAS broj 9032-82-0
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
ATP + riboflavin ADP + FMN

Kofaktori FMN i FAD učestvuju u brojnim procesima u svim organizmima, uključujući mitohondrijski elektronski transport, fotosintezu, masna-kiselinsku oksidaciju, i metabolizam vitamina B6, vitamina B12 i folata.

ReferenceUredi

  1. Chassy, B.M., Arsenis, C. and McCormick, D.B. (1965). „The effect of the length of the side chain of flavins on reactivity with flavokinase”. J. Biol. Chem. 240: 1338-1340. PMID 14284745. 
  2. Giri, K.V., Krishnaswamy, P.R. and Rao, N.A. (1958). „Studies on plant flavokinase”. Biochem. J. 70: 66-71. PMID 13584303. 
  3. Kearney, E.B. (1952). „The interaction of yeast flavokinase with riboflavin analogues”. J. Biol. Chem. 194: 747-754. PMID 14927668. 
  4. McCormick, D.B. and Butler, R.C. (1962). „Substrate specificity of liver flavokinase”. Biochim. Biophys. Acta 65: 326-332. 
  5. Sandoval, F.J. and Roje, S. (2005). „An FMN hydrolase is fused to a riboflavin kinase homolog in plants”. J. Biol. Chem. 280: 38337-38345. PMID 16183635. 
  6. Solovieva, I.M., Tarasov, K.V. and Perumov, D.A. (2003). „Main physicochemical features of monofunctional flavokinase from Bacillus subtilis”. Biochemistry (Mosc) 68: 177-181. PMID 12693963. 
  7. Solovieva, I.M., Kreneva, R.A., Leak, D.J. and Perumov, D.A. (1999). „The ribR gene encodes a monofunctional riboflavin kinase which is involved in regulation of the Bacillus subtilis riboflavin operon”. Microbiology 145: 67-73. PMID 10206712. 

LiteraturaUredi

Spoljašnje vezeUredi